Nature Communications (May 2020)

Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

  • Alessandro Piai,
  • Qingshan Fu,
  • Yongfei Cai,
  • Fadi Ghantous,
  • Tianshu Xiao,
  • Md Munan Shaik,
  • Hanqin Peng,
  • Sophia Rits-Volloch,
  • Wen Chen,
  • Michael S. Seaman,
  • Bing Chen,
  • James J. Chou

DOI
https://doi.org/10.1038/s41467-020-16165-0
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 12

Abstract

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HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic tail (CT), and show that the CT folds into membrane attached amphipathic helices that wrap around the TMD thereby forming a support baseplate for the rest of Env, and they also provide insights into the dynamic coupling across the TMD between the ectodomain and CT.